U17L6_HUMAN
ID U17L6_HUMAN Reviewed; 398 AA.
AC Q6QN14;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein 6;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 17-like protein 6;
DE AltName: Full=Ubiquitin thioesterase 17-like protein 6;
DE AltName: Full=Ubiquitin-specific-processing protease 17-like protein 6;
GN Name=USP17L6P; Synonyms=USP17C, USP17D, USP17N;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF CYS-89, AND SUBCELLULAR LOCATION.
RX PubMed=17109758; DOI=10.1186/1471-2164-7-292;
RA Shin J.-M., Yoo K.-J., Kim M.-S., Kim D., Baek K.-H.;
RT "Hyaluronan- and RNA-binding deubiquitinating enzymes of USP17 family
RT members associated with cell viability.";
RL BMC Genomics 7:292-292(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=15780755; DOI=10.1016/j.ygeno.2004.11.013;
RA Burrows J.F., McGrattan M.J., Johnston J.A.;
RT "The DUB/USP17 deubiquitinating enzymes, a multigene family within a
RT tandemly repeated sequence.";
RL Genomics 85:524-529(2005).
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes that
CC may include cell proliferation, progression through the cell cycle,
CC cell migration, and the cellular response to viral infection. Seems to
CC be non-functional in the regulation of apoptosis.
CC {ECO:0000269|PubMed:17109758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:17109758};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17109758}. Cytoplasm
CC {ECO:0000269|PubMed:17109758}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: The RS447 megasatellite DNA is a highly polymorphic conserved
CC tandem repetitive sequence which contains a copy of the USP17 gene. It
CC is present with an interindividual variation in copy number, ranging
CC from 20 to 103, and can be found in the genome both on chromosome 4 and
CC chromosome 8. The high similarity between the UPS17-like genes makes
CC impossible to clearly assign data to one of the genes of the family.
CC Oligonucleotides designed in RNAi experiments are for instance not
CC specific of a given UPS17-like gene. {ECO:0000305}.
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DR EMBL; AY533200; AAS59847.1; -; mRNA.
DR EMBL; AC116655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6QN14; -.
DR SMR; Q6QN14; -.
DR MEROPS; C19.A82; -.
DR MEROPS; C19.A87; -.
DR BioMuta; HGNC:37179; -.
DR DMDM; 187663985; -.
DR PeptideAtlas; Q6QN14; -.
DR PRIDE; Q6QN14; -.
DR GeneCards; USP17L6P; -.
DR HGNC; HGNC:37179; USP17L6P.
DR neXtProt; NX_Q6QN14; -.
DR InParanoid; Q6QN14; -.
DR PhylomeDB; Q6QN14; -.
DR Pharos; Q6QN14; Tbio.
DR PRO; PR:Q6QN14; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q6QN14; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..398
FT /note="Ubiquitin carboxyl-terminal hydrolase 17-like
FT protein 6"
FT /id="PRO_0000331648"
FT DOMAIN 80..375
FT /note="USP"
FT ACT_SITE 89
FT /note="Nucleophile"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MUTAGEN 89
FT /note="C->S: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17109758"
FT CONFLICT 9
FT /note="R -> G (in Ref. 1; AAS59847)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="S -> P (in Ref. 1; AAS59847)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> T (in Ref. 1; AAS59847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44690 MW; 350E31797F7EFD44 CRC64;
MEDDSLYLRG EWQFNHFSKL TSSRPDAAFA EIQRTSLPEK SPLSCETRVD LCDDLAPVAR
QLAPREKLPL SSRRPAAVGA GLQNMGNTCY VNASLQCLTY TPPLANYMLS REHSQTCHRH
KGCMLCTMQA HITRALHNPG HVIQPSQALA AGFHRGKQED AHEFLMFTVD AMKKACLPGH
KQVDHHSKDT TLIHQIFGGY WRSQIKCLHC HGISDTFDPY LDIALDIQAA QSVQQALEQL
VKPEELNGEN AYHCGVCLQR APASKTLTLH TSAKVLILVL KRFSDVTGNK IAKNVQYPEC
LDMQPYMSQQ NTGPLVYVLY AVLVHAGWSC HNGHYFSYVK AQEGQWYKMD DAEVTASSIT
SVLSQQAYVL FYIQKSEWER HSESVSRGRE PRALGSED
